Membrane lipid composition protects Entamoeba histolytica from self‐destruction by its pore‐forming toxins

FEBS Letters

Andrä, Jörg²  Berninghausen, Otto³  Leippe, Matthias¹ 

[1] Zoological Institute, University of Kiel, Olshausenstr. 40, 24098 Kiel, Germany;Division of Biophysics, Forschungszentrum Borstel, Leibniz Center for Medicine and Biosciences, Parkallee 10, 23845 Borstel, Germany;Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany

关键词: Amoebapore;    Antimicrobial peptide;    Self-protection;    Cholesterol;    Pore-forming protein;    Lipid raft;    Entamoeba histolytica;    CAEP;    ceramide aminoethylphosphonate;    CAEphosphate;    N-acyl-sphingosylphosphorylethanolamine;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    PG;    phosphatidylglycerol;    PI;    phosphatidylinositol;    PS;    phosphatidylserine;    TRITC;    tetramethylrhodamine isothiocyanate;   

DOI  :  10.1016/S0014-5793(04)00324-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protozoan parasite and human pathogen Entamoeba histolytica is protected against killing by its own lytic effector proteins. Amoebae withstand doses of amoebapores, their pore-forming polypeptides, that readily kill human Jurkat T cells. Moreover, the polypeptides do not bind to the amoebic surface membrane as evidenced by using fluorescently labelled amoebapores and confocal laser microscopy. Experiments employing liposomes as a minimalistic membrane system and the major isoform amoebapore A revealed that the lipid composition of amoebic membranes prevents binding of the cytolytic molecule and that both the phospholipid ingredients and the high content of cholesterol contributes to the protection of the toxin-producing cell.

【 授权许可】

Unknown